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23 Cards in this Set
- Front
- Back
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folding |
arriving at the “correct” combinations of phi and psi angles for every residue in the sequence |
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hydrophobic groups |
rapidly bury themselves from water to form molten globule |
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molten globule |
hydrophobic core with a lot of freedom of motion |
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upper bars on hydropathy plot |
found in the interier of protein |
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lower bars on hydropathy plot |
are exterior residues |
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thermo of protein folding |
ΔG = ΔH – TΔS |
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ΔH is negative |
due to lower dielectric constantinside the protein (making bonds is favorable) |
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limiting phi and psi angles |
into native conformation is entropically unfavorable |
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Lymphotactin |
exists in 2 conformations (both in equilibrium) |
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contribute to protein stability |
salt links and electrostatic interactions |
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proteins arent |
static |
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globular proteins |
-compact, spherical -water soluble |
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fibrous proteins |
-polypeptide chains are assembles into elongated rope like or sheet like structure - water insoluble -have repeating motifs of secondary structure |
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Collagen |
-every 3rd residue is Gly -has Pro and Hyp bc inflexible -only glycine can fit in interior |
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if G mutated to S in collagen |
can lead to osteogenesis imperfecta |
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Coiled coils in alpha-keratin |
- 2 right handed alpha helices coiled around each other in left handed direction -supercoiled |
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alpha-keratin |
-fibrous protein, insoluble, elongated 3d - found in hair, quills, claws, and horns -crosslinked by disulfide bonds |
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Anfinsen's exp |
unfolding and refolding RNase with UREA as denaturing agent (8M) and 2-ME as reducing agent |
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Heat shock proteins (HSP70) |
-J protein - chaperones to prevent denature or aggregation |
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CREB |
-cAMP response element binding protein -flexible to interact -can bind w/ high specificity w/ modest affinity |
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Intrinsically disordered proteins (IDP) |
-1/3 mammal proteins have - lack hydrophobic core - lots of Pro and polar aa |
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amaloidoses |
A core of β-strands is alignedperpendicularly to the fibril axis formingextended regular β-sheets |
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Prions |
-very scary cause mad cow - PrPSC, can aggregate to form “cross-beta” structures, and small aggregates |
